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Aug 2020 DOI 10.14302/issn.2835-513X.ijl-20-3457
Gupta AnjuCorresponding author
Department of Mechanical, Industrial and Manufacturing Engineering, University of Toledo, Toledo, OH 43614, USA
PEGylation is a well-established strategy for improving the target specificity, circulation time and stability of liposomes, thereby improving their stealth properties. This brief review provides an insight on the composition of PEGylated liposomes and the characteristics that dictate the functionality of PEGylated liposomes such as surface density, molecular weight, presence of linkers and acyl groups. Physicochemical techniques used to characterize the PEG liposomes and test their stability are also discussed along with their clinical implications. This review provides the readers with a broad range of understanding of various PEGylated lipids, techniques to access their stability in liposomal formulations and state-of -the-art development of PEGylated liposomal formulations.
Jul 2020 DOI 10.14302/issn.2690-4829.jen-20-3480
Brumm PhillipCorresponding author
C5-6 Technologies LLC, 5627 Old Oak Drive, Fitchburg, WI 53711, USA
Conversion of biomass into fermentable sugars is a major requirement for successful and cost-effective biofuels production. The conversion of xylan to sugars requires multiple enzymes including α-glucuronidase. Here we report the cloning, expression, purification and characterization of the α-glucuronidase from Dictyoglomusturgidum(DtuAgu). DtuAgu is an intracellular protein of 685 amino acids and a predicted molecular weight of 79.4 kD. Enzymatic activity was optimum between pH 7.0 and 8.0 and at 85°C. The specific activity of the enzyme was 10 u/mg when measured using mixed aldouronic acids. The specific activity on isolated glucuronoxylan was approximately 20% of the value obtained with xylooligosaccharides. DtuAgu significantly improved xylan conversion to xylose when evaluated using two mixtures of thermostable bacterial enzymes and two sources of xylan. DtuAgu has the potential to be a key player in thermostable enzyme cocktails for the conversion to biomass to biofuels.α
Mar 2019 DOI 10.14302/issn.2471-2140.jaa-19-2699
M.M. Masoud HassanCorresponding author
Molecular Biology Department, National Research Centre, El-Tahrir st., Dokki, Giza, Egypt.
Xanthine oxidase is a commercially important enzyme with wide area of medical applications to develop diagnostic kits. Xanthine oxidase was extracted, purified and characterized from sheep liver (SLXO). The purification procedure involved acetone precipitation and chromatography on DEAE-cellulose and Sephacryl S-300 columns. The sheep liver xanthine oxidase was homogeneously purified 31.8 folds with 3.5 U/mg specific activity and 24.1% recovery. SLXO native molecular weight was 150 kDa and on SDS-PAGE appeared as single major band of 75 kDa representing a homodimer protein. Isoelectric focusing of the purified SLXO resolved into two closely related isoforms with pI values of 5.6 and 5.8. The apparent Km for xanthine oxidase at optimum pH 7.6 was found to be 0.9 mM xanthine. FeCl2 and NiCl2 increased the activity of SLXO, while CuCl2 and ZnCl2 were found to be potent inhibitors of the purified enzyme. Allopurinol inhibits SLXO competitively with one binding site on the purified molecule and Ki value of 0.06 mM.